GenomeNet

Database: UniProt
Entry: Q39191
LinkDB: Q39191
Original site: Q39191 
ID   WAK1_ARATH              Reviewed;         735 AA.
AC   Q39191; O81820; Q56WT2; Q9LMP0;
DT   17-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT   17-OCT-2006, sequence version 2.
DT   13-FEB-2019, entry version 144.
DE   RecName: Full=Wall-associated receptor kinase 1;
DE            EC=2.7.11.-;
DE   Flags: Precursor;
GN   Name=WAK1; Synonyms=PRO25; OrderedLocusNames=At1g21250;
GN   ORFNames=F16F4.6;
OS   Arabidopsis thaliana (Mouse-ear cress).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliophyta; eudicotyledons; Gunneridae;
OC   Pentapetalae; rosids; malvids; Brassicales; Brassicaceae; Camelineae;
OC   Arabidopsis.
OX   NCBI_TaxID=3702;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], TISSUE SPECIFICITY, AND INDUCTION.
RX   PubMed=10380805; DOI=10.1023/A:1006197318246;
RA   He Z.-H., Cheeseman I., He D., Kohorn B.D.;
RT   "A cluster of five cell wall-associated receptor kinase genes, Wak1-5,
RT   are expressed in specific organs of Arabidopsis.";
RL   Plant Mol. Biol. 39:1189-1196(1999).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=11130712; DOI=10.1038/35048500;
RA   Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S.,
RA   White O., Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y.,
RA   Buehler E., Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W.,
RA   Chung M.K., Conn L., Conway A.B., Conway A.R., Creasy T.H., Dewar K.,
RA   Dunn P., Etgu P., Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y.,
RA   Gill J.E., Goldsmith A.D., Haas B., Hansen N.F., Hughes B., Huizar L.,
RA   Hunter J.L., Jenkins J., Johnson-Hopson C., Khan S., Khaykin E.,
RA   Kim C.J., Koo H.L., Kremenetskaia I., Kurtz D.B., Kwan A., Lam B.,
RA   Langin-Hooper S., Lee A., Lee J.M., Lenz C.A., Li J.H., Li Y.-P.,
RA   Lin X., Liu S.X., Liu Z.A., Luros J.S., Maiti R., Marziali A.,
RA   Militscher J., Miranda M., Nguyen M., Nierman W.C., Osborne B.I.,
RA   Pai G., Peterson J., Pham P.K., Rizzo M., Rooney T., Rowley D.,
RA   Sakano H., Salzberg S.L., Schwartz J.R., Shinn P., Southwick A.M.,
RA   Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA   Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M.,
RA   Wu D., Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT   "Sequence and analysis of chromosome 1 of the plant Arabidopsis
RT   thaliana.";
RL   Nature 408:816-820(2000).
RN   [3]
RP   GENOME REANNOTATION.
RC   STRAIN=cv. Columbia;
RX   PubMed=27862469; DOI=10.1111/tpj.13415;
RA   Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA   Town C.D.;
RT   "Araport11: a complete reannotation of the Arabidopsis thaliana
RT   reference genome.";
RL   Plant J. 89:789-804(2017).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=14593172; DOI=10.1126/science.1088305;
RA   Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J.,
RA   Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F.,
RA   Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G.,
RA   Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J.,
RA   Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y.,
RA   Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P.,
RA   Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F.,
RA   Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M.,
RA   Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J.,
RA   Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T.,
RA   Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y.,
RA   Yuan S., Shinozaki K., Davis R.W., Theologis A., Ecker J.R.;
RT   "Empirical analysis of transcriptional activity in the Arabidopsis
RT   genome.";
RL   Science 302:842-846(2003).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 50-735, AND TISSUE SPECIFICITY.
RC   STRAIN=cv. Columbia;
RX   PubMed=1438303; DOI=10.1073/pnas.89.22.10989;
RA   Kohorn B.D., Lane S., Smith T.A.;
RT   "An Arabidopsis serine/threonine kinase homologue with an epidermal
RT   growth factor repeat selected in yeast for its specificity for a
RT   thylakoid membrane protein.";
RL   Proc. Natl. Acad. Sci. U.S.A. 89:10989-10992(1992).
RN   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 419-735.
RC   STRAIN=cv. Columbia;
RA   Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
RA   Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
RA   Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
RA   Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J.,
RA   Hayashizaki Y., Shinozaki K.;
RT   "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
RL   Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
RN   [7]
RP   SUBCELLULAR LOCATION.
RX   PubMed=8702686; DOI=10.1074/jbc.271.33.19789;
RA   He Z.-H., Fujiki M., Kohorn B.D.;
RT   "A cell wall-associated, receptor-like protein kinase.";
RL   J. Biol. Chem. 271:19789-19793(1996).
RN   [8]
RP   TISSUE SPECIFICITY, AND INDUCTION.
RX   PubMed=9681026; DOI=10.1046/j.1365-313X.1998.00092.x;
RA   He Z.-H., He D., Kohorn B.D.;
RT   "Requirement for the induced expression of a cell wall associated
RT   receptor kinase for survival during the pathogen response.";
RL   Plant J. 14:55-63(1998).
RN   [9]
RP   INDUCTION.
RX   PubMed=11027363; DOI=10.1073/pnas.97.21.11655;
RA   Schenk P.M., Kazan K., Wilson I., Anderson J.P., Richmond T.,
RA   Somerville S.C., Manners J.M.;
RT   "Coordinated plant defense responses in Arabidopsis revealed by
RT   microarray analysis.";
RL   Proc. Natl. Acad. Sci. U.S.A. 97:11655-11660(2000).
RN   [10]
RP   INTERACTION WITH GRP3 AND GRP3S, INDUCTION, AND TISSUE SPECIFICITY.
RX   PubMed=11335717; DOI=10.1074/jbc.M101283200;
RA   Park A.R., Cho S.K., Yun U.J., Jin M.Y., Lee S.H.,
RA   Sachetto-Martins G., Park O.K.;
RT   "Interaction of the Arabidopsis receptor protein kinase Wak1 with a
RT   glycine-rich protein, AtGRP-3.";
RL   J. Biol. Chem. 276:26688-26693(2001).
RN   [11]
RP   FUNCTION, INDUCTION, DEVELOPMENTAL STAGE, AND BINDING TO PECTIN.
RX   PubMed=11226187; DOI=10.1105/tpc.13.2.303;
RA   Wagner T.A., Kohorn B.D.;
RT   "Wall-associated kinases are expressed throughout plant development
RT   and are required for cell expansion.";
RL   Plant Cell 13:303-318(2001).
RN   [12]
RP   INTERACTION WITH KAPP.
RX   PubMed=11554472; DOI=10.1023/A:1010691701578;
RA   Anderson C.M., Wagner T.A., Perret M., He Z.-H., He D., Kohorn B.D.;
RT   "WAKs: cell wall-associated kinases linking the cytoplasm to the
RT   extracellular matrix.";
RL   Plant Mol. Biol. 47:197-206(2001).
RN   [13]
RP   GENE FAMILY ORGANIZATION.
RX   PubMed=12068092; DOI=10.1104/pp.011028;
RA   Verica J.A., He Z.-H.;
RT   "The cell wall-associated kinase (WAK) and WAK-like kinase gene
RT   family.";
RL   Plant Physiol. 129:455-459(2002).
RN   [14]
RP   FUNCTION, AND INTERACTION WITH OEE2.
RX   PubMed=12767910; DOI=10.1016/S0006-291X(03)00851-9;
RA   Yang E.J., Oh Y.A., Lee E.S., Park A.R., Cho S.K., Yoo Y.J.,
RA   Park O.K.;
RT   "Oxygen-evolving enhancer protein 2 is phosphorylated by glycine-rich
RT   protein 3/wall-associated kinase 1 in Arabidopsis.";
RL   Biochem. Biophys. Res. Commun. 305:862-868(2003).
RN   [15]
RP   FUNCTION, AND INDUCTION.
RX   PubMed=12913180; DOI=10.1104/pp.103.022129;
RA   Sivaguru M., Ezaki B., He Z.-H., Tong H.-Y., Osawa H., Baluska F.,
RA   Volkmann D., Matsumoto H.;
RT   "Aluminum-induced gene expression and protein localization of a cell
RT   wall-associated receptor kinase in Arabidopsis.";
RL   Plant Physiol. 132:2256-2266(2003).
RN   [16]
RP   BINDING TO PECTIN.
RX   PubMed=15769808; DOI=10.1093/pcp/pci026;
RA   Decreux A., Messiaen J.;
RT   "Wall-associated kinase WAK1 interacts with cell wall pectins in a
RT   calcium-induced conformation.";
RL   Plant Cell Physiol. 46:268-278(2005).
RN   [17]
RP   BINDING TO PECTIN, AND MUTAGENESIS OF ARG-67; ARG-91; LYS-101; LYS-102
RP   AND ARG-166.
RX   PubMed=16631829; DOI=10.1016/j.phytochem.2006.03.009;
RA   Decreux A., Thomas A., Spies B., Brasseur R., Van Cutsem P.,
RA   Messiaen J.;
RT   "In vitro characterization of the homogalacturonan-binding domain of
RT   the wall-associated kinase WAK1 using site-directed mutagenesis.";
RL   Phytochemistry 67:1068-1079(2006).
CC   -!- FUNCTION: Serine/threonine-protein kinase that may function as a
CC       signaling receptor of extracellular matrix component. Binding to
CC       pectin may have significance in the control of cell expansion,
CC       morphogenesis and development. Required during plant's response to
CC       pathogen infection and in plant defense against heavy metal
CC       toxicity. Phosphorylates the oxygen-evolving enhancer protein 2
CC       (OEE2) in an GRP-3-dependent manner. {ECO:0000269|PubMed:11226187,
CC       ECO:0000269|PubMed:12767910, ECO:0000269|PubMed:12913180}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-
CC         [protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-
CC         COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999,
CC         ChEBI:CHEBI:30616, ChEBI:CHEBI:83421, ChEBI:CHEBI:456216;
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-
CC         threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060,
CC         Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013,
CC         ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216;
CC   -!- SUBUNIT: Interacts with the glycine-rich proteins GRP3 and GRP3S,
CC       and the type 2C protein phosphatase KAPP. Component of a 500 kDa
CC       complex, composed of WAK1, GRP3 and KAPP. Interacts with the
CC       oxygen-evolving enhancer protein 2 (OEE2).
CC       {ECO:0000269|PubMed:11335717, ECO:0000269|PubMed:11554472,
CC       ECO:0000269|PubMed:12767910}.
CC   -!- INTERACTION:
CC       Q9SL15:GRP3; NbExp=5; IntAct=EBI-2320121, EBI-1541435;
CC       Q9ZSJ6:GRP3S; NbExp=2; IntAct=EBI-2320121, EBI-2319984;
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000269|PubMed:8702686};
CC       Single-pass type I membrane protein {ECO:0000269|PubMed:8702686}.
CC   -!- TISSUE SPECIFICITY: Predominantly expressed in green tissues such
CC       as stems and leaves. Detected at organ junctions.
CC       {ECO:0000269|PubMed:10380805, ECO:0000269|PubMed:11335717,
CC       ECO:0000269|PubMed:1438303, ECO:0000269|PubMed:9681026}.
CC   -!- DEVELOPMENTAL STAGE: Expressed in shoot and root apical meristems,
CC       and in expanding leaves and sepals. {ECO:0000269|PubMed:11226187}.
CC   -!- INDUCTION: Induced by salicylic acid (SA) or INA, methyl
CC       jasmonate, ethylene, wounding and pathogen infection. Accumulated
CC       in roots after Aluminum exposure. Up-regulated by GRP3.
CC       {ECO:0000269|PubMed:10380805, ECO:0000269|PubMed:11027363,
CC       ECO:0000269|PubMed:11226187, ECO:0000269|PubMed:11335717,
CC       ECO:0000269|PubMed:12913180, ECO:0000269|PubMed:9681026}.
CC   -!- MISCELLANEOUS: Binding to polygalacturonic acid (PGA) multimers is
CC       calcium-dependent.
CC   -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr
CC       protein kinase family. {ECO:0000255|PROSITE-ProRule:PRU00159}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAA32844.1; Type=Frameshift; Positions=65, 117; Evidence={ECO:0000305};
CC       Sequence=AAF81356.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC   -!- WEB RESOURCE: Name=PlantP kinase Classification PPC;
CC       URL="http://plantsp.genomics.purdue.edu/family/class.html";
DR   EMBL; AJ009696; CAA08794.1; -; Genomic_DNA.
DR   EMBL; AC036104; AAF81356.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; CP002684; AEE30079.1; -; Genomic_DNA.
DR   EMBL; AY039917; AAK64021.1; -; mRNA.
DR   EMBL; BT001967; AAN71966.1; -; mRNA.
DR   EMBL; L04999; AAA32844.1; ALT_FRAME; mRNA.
DR   EMBL; AK221950; BAD94420.1; -; mRNA.
DR   PIR; H86345; A46373.
DR   RefSeq; NP_564137.1; NM_101978.5.
DR   UniGene; At.23880; -.
DR   ProteinModelPortal; Q39191; -.
DR   SMR; Q39191; -.
DR   BioGrid; 23960; 3.
DR   IntAct; Q39191; 3.
DR   STRING; 3702.AT1G21250.1; -.
DR   iPTMnet; Q39191; -.
DR   PaxDb; Q39191; -.
DR   PRIDE; Q39191; -.
DR   EnsemblPlants; AT1G21250.1; AT1G21250.1; AT1G21250.
DR   GeneID; 838721; -.
DR   Gramene; AT1G21250.1; AT1G21250.1; AT1G21250.
DR   KEGG; ath:AT1G21250; -.
DR   Araport; AT1G21250; -.
DR   TAIR; locus:2014902; AT1G21250.
DR   eggNOG; ENOG410IM0I; Eukaryota.
DR   eggNOG; COG0515; LUCA.
DR   HOGENOM; HOG000116550; -.
DR   InParanoid; Q39191; -.
DR   OMA; VISATWI; -.
DR   OrthoDB; 496739at2759; -.
DR   PhylomeDB; Q39191; -.
DR   PRO; PR:Q39191; -.
DR   Proteomes; UP000006548; Chromosome 1.
DR   Genevisible; Q39191; AT.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0009505; C:plant-type cell wall; IDA:TAIR.
DR   GO; GO:0005886; C:plasma membrane; ISS:TAIR.
DR   GO; GO:0005773; C:vacuole; IDA:TAIR.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR   GO; GO:0016301; F:kinase activity; ISS:TAIR.
DR   GO; GO:0030247; F:polysaccharide binding; IEA:InterPro.
DR   GO; GO:0004674; F:protein serine/threonine kinase activity; IBA:GO_Central.
DR   GO; GO:0050832; P:defense response to fungus; IMP:TAIR.
DR   GO; GO:0009751; P:response to salicylic acid; IEP:TAIR.
DR   GO; GO:0009615; P:response to virus; IEP:TAIR.
DR   InterPro; IPR001881; EGF-like_Ca-bd_dom.
DR   InterPro; IPR000742; EGF-like_dom.
DR   InterPro; IPR000152; EGF-type_Asp/Asn_hydroxyl_site.
DR   InterPro; IPR018097; EGF_Ca-bd_CS.
DR   InterPro; IPR011009; Kinase-like_dom_sf.
DR   InterPro; IPR000719; Prot_kinase_dom.
DR   InterPro; IPR001245; Ser-Thr/Tyr_kinase_cat_dom.
DR   InterPro; IPR008271; Ser/Thr_kinase_AS.
DR   InterPro; IPR025287; WAK_GUB.
DR   Pfam; PF07645; EGF_CA; 1.
DR   Pfam; PF13947; GUB_WAK_bind; 1.
DR   Pfam; PF07714; Pkinase_Tyr; 1.
DR   SMART; SM00181; EGF; 2.
DR   SMART; SM00179; EGF_CA; 2.
DR   SMART; SM00220; S_TKc; 1.
DR   SUPFAM; SSF56112; SSF56112; 1.
DR   PROSITE; PS00010; ASX_HYDROXYL; 1.
DR   PROSITE; PS01186; EGF_2; 1.
DR   PROSITE; PS50026; EGF_3; 2.
DR   PROSITE; PS01187; EGF_CA; 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR   PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE   1: Evidence at protein level;
KW   ATP-binding; Calcium; Complete proteome; Disulfide bond;
KW   EGF-like domain; Glycoprotein; Kinase; Membrane; Nucleotide-binding;
KW   Phosphoprotein; Reference proteome; Repeat;
KW   Serine/threonine-protein kinase; Signal; Transferase; Transmembrane;
KW   Transmembrane helix.
FT   SIGNAL        1     24       {ECO:0000255}.
FT   CHAIN        25    735       Wall-associated receptor kinase 1.
FT                                /FTId=PRO_0000253300.
FT   TOPO_DOM     25    331       Extracellular. {ECO:0000255}.
FT   TRANSMEM    332    352       Helical. {ECO:0000255}.
FT   TOPO_DOM    353    735       Cytoplasmic. {ECO:0000255}.
FT   DOMAIN      234    281       EGF-like 1. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00076}.
FT   DOMAIN      282    328       EGF-like 2; calcium-binding.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DOMAIN      409    692       Protein kinase. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00159}.
FT   NP_BIND     415    423       ATP. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00159}.
FT   REGION       67    254       Polygalacturonic acid-binding.
FT   ACT_SITE    534    534       Proton acceptor. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00159, ECO:0000255|PROSITE-
FT                                ProRule:PRU10027}.
FT   BINDING     437    437       ATP. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00159}.
FT   MOD_RES     398    398       Phosphothreonine.
FT                                {ECO:0000250|UniProtKB:O48814}.
FT   MOD_RES     482    482       Phosphotyrosine.
FT                                {ECO:0000250|UniProtKB:O48814}.
FT   MOD_RES     568    568       Phosphothreonine.
FT                                {ECO:0000250|UniProtKB:O48814}.
FT   MOD_RES     573    573       Phosphothreonine.
FT                                {ECO:0000250|UniProtKB:O48814}.
FT   MOD_RES     581    581       Phosphotyrosine.
FT                                {ECO:0000250|UniProtKB:O48814}.
FT   CARBOHYD     38     38       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD     56     56       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD     80     80       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD     90     90       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    113    113       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    140    140       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    209    209       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    235    235       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    250    250       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    296    296       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   DISULFID    238    253       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID    247    264       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID    266    280       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID    286    303       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID    297    312       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID    314    327       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   MUTAGEN      67     67       R->Q: Decreases the binding to dimeric
FT                                PGA; when associated with T-101 and T-
FT                                102. {ECO:0000269|PubMed:16631829}.
FT   MUTAGEN      91     91       R->Q: Decreases the binding to dimeric
FT                                PGA; when associated with Q-166.
FT                                Decreases the binding to multimeric PGA;
FT                                when associated with T-101; T-102 and Q-
FT                                166. {ECO:0000269|PubMed:16631829}.
FT   MUTAGEN     101    101       K->T: Decreases the binding to dimeric
FT                                PGA; when associated with Q-67 and T-102.
FT                                Abolishes the binding to dimeric PGA;
FT                                when associated with T-102 and Q-166.
FT                                {ECO:0000269|PubMed:16631829}.
FT   MUTAGEN     102    102       K->T: Decreases the binding to dimeric
FT                                PGA; when associated with Q-67 and T-101.
FT                                Abolishes the binding to dimeric PGA;
FT                                when associated with T-101 and Q-166.
FT                                {ECO:0000269|PubMed:16631829}.
FT   MUTAGEN     166    166       R->Q: Decreases the binding to dimeric
FT                                PGA; when associated with Q-91. Abolishes
FT                                the binding to dimeric PGA; when
FT                                associated with T-101 and T-202.
FT                                {ECO:0000269|PubMed:16631829}.
FT   CONFLICT    212    212       S -> C (in Ref. 5; AAA32844).
FT                                {ECO:0000305}.
FT   CONFLICT    244    244       T -> I (in Ref. 5; AAA32844).
FT                                {ECO:0000305}.
FT   CONFLICT    386    387       Missing (in Ref. 5; AAA32844).
FT                                {ECO:0000305}.
FT   CONFLICT    458    458       S -> P (in Ref. 5; AAA32844).
FT                                {ECO:0000305}.
FT   CONFLICT    663    668       RLMGEE -> TNGRG (in Ref. 5; AAA32844).
FT                                {ECO:0000305}.
SQ   SEQUENCE   735 AA;  81211 MW;  AAD41A28296093E6 CRC64;
     MKVQEGLFLV AIFFSLACTQ LVKGQHQPGE NCQNKCGNIT IEYPFGISSG CYYPGNESFS
     ITCKEDRPHV LSDIEVANFN HSGQLQVLLN RSSTCYDEQG KKTEEDSSFT LENLSLSANN
     KLTAVGCNAL SLLDTFGMQN YSTACLSLCD SPPEADGECN GRGCCRVDVS APLDSYTFET
     TSGRIKHMTS FHDFSPCTYA FLVEDDKFNF SSTEDLLNLR NVMRFPVLLD WSVGNQTCEQ
     VGSTSICGGN STCLDSTPRN GYICRCNEGF DGNPYLSAGC QDVNECTTSS TIHRHNCSDP
     KTCRNKVGGF YCKCQSGYRL DTTTMSCKRK EFAWTTILLV TTIGFLVILL GVACIQQRMK
     HLKDTKLREQ FFEQNGGGML TQRLSGAGPS NVDVKIFTED GMKKATNGYA ESRILGQGGQ
     GTVYKGILPD NSIVAIKKAR LGDSSQVEQF INEVLVLSQI NHRNVVKLLG CCLETEVPLL
     VYEFITNGTL FDHLHGSMID SSLTWEHRLK IAIEVAGTLA YLHSSASIPI IHRDIKTANI
     LLDVNLTAKV ADFGASRLIP MDKEELETMV QGTLGYLDPE YYNTGLLNEK SDVYSFGVVL
     MELLSGQKAL CFKRPQSSKH LVSYFATATK ENRLDEIIGG EVMNEDNLKE IQEAARIAAE
     CTRLMGEERP RMKEVAAKLE ALRVEKTKHK WSDQYPEENE HLIGGHILSA QGETSSSIGY
     DSIKNVAILD IETGR
//
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